The DOI matches its Crossref record; 63 of the 64 references it cites were found in a registry or an index, and 1 are not checked yet.
Computational Design and Experimental Characterization of Peptides Intended for pH-Dependent Membrane Insertion and Pore Formation
Open accessAbstract
There are many opportunities to use macromolecules, such as peptides and oligonucleotides, for intracellular applications. Despite this, general methods for delivering these molecules to the cytosol in a safe and efficient manner are not available. Efforts to develop a variety of intracellular drug delivery systems such as viral vectors, lipoplexes, nanoparticles, and amphiphilic peptides have been made, but various challenges such as delivery efficiency, toxicity, and controllability remain. A central challenge is the ability to selectively perturb, not destroy, the membrane to facilitate cargo introduction. Herein, we describe our efforts to design and characterize peptides that form pores inside membranes at acidic pH, so-called pH-switchable pore formation (PSPF) peptides, as a potential means for facilitating cargo translocation through membranes. Consistent with pore formation, these peptides exhibit low-pH-triggered selective release of ATP and miRNA, but not hemoglobin, from red blood cells. Consistent with these observations, biophysical studies (tryptophan fluorescence, circular dichroism, size-exclusion chromatography, analytical ultracentrifugation, and attenuated total reflectance Fourier transformed infrared spectroscopy) show that decreased pH destabilizes the PSPF peptides in aqueous systems while promoting their membrane insertion. Together, these results suggest that reduced pH drives insertion of PSPF peptides into membranes, leading to target-specific escape through a proposed pore formation mechanism.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Achieving the desired balance between multiple target coiled-coil states often requires several rounds of trial-and-error and a detailed understanding of the energetic factors that discriminate between alternative topologies and oligomerization states.
“While this has been accomplished in a number of cases,18−31 achieving the desired balance between multiple target coiled-coil states often requires several rounds of trial-and-error and a detailed understanding of the energetic factors that discriminate between alternative topologies and oligomerization states.”
From Assessment of the Topology and Oligomerisation States of Coiled Coils Using Metadynamics with Conformational Restraints (2025) · cites this paper as [23]
Split into 2 atoms — 0 confirmed, 2 partially supported, 0 disputed, 0 misattributed, 0 unverifiable. Expand the claim to see per-atom verdicts.
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Boussif, O., Lezoualc’h, F., Zanta, M. A., Djavaheri‐Mergny, M., Scherman, D., DEMENEIX, B. A., & Behr, J. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.16.7297 · Cited by 6,256
Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
Brogden, K. A. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1098 · Cited by 5,829
ACIDIFICATION OF THE ENDOCYTIC AND EXOCYTIC PATHWAYS
Mellman, I., Fuchs, R., & Helenius, A. (1986) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.55.070186.003311 · Cited by 2,045
Shai, Y. (1999) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(99)00200-x · Cited by 1,904
MEMBRANE PROTEIN FOLDING AND STABILITY: Physical Principles
White, S. H., & Wimley, W. C. (1999) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.28.1.319 · Cited by 1,767
The packing of α-helices: simple coiled-coils
Crick, F. H. C. (1953) · Acta Crystallographica · doi:10.1107/s0365110x53001964 · Cited by 1,578
RNAi-mediated gene silencing in non-human primates
Zimmermann, T. S., Lee, A. C. H., Akinc, A., Bramlage, B., Bumcrot, D., Fedoruk, M. N., Harborth, J., Heyes, J. A., Jeffs, L. B., John, M., et al. (2006) · Nature · doi:10.1038/nature04688 · Cited by 1,357
Coiled coils: new structures and new functions
Lupas, A. N. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)10052-9 · Cited by 1,321
A Thermodynamic Scale for the Helix-Forming Tendencies of the Commonly Occurring Amino Acids
O’Neil, K. T., & DeGrado, W. F. (1990) · Science · doi:10.1126/science.2237415 · Cited by 1,186
Self-citationCoiled coils: new structures and new functions
Lupas, A. N. (1996) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(96)10052-9 · Cited by 836
α‐Helical coiled coils and bundles: How to design an α‐helical protein
Cohen, C., & Parry, D. A. D. (1990) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340070102 · Cited by 713
RECENT APPROACHES TO INTRACELLULAR DELIVERY OF DRUGS AND DNA AND ORGANELLE TARGETING
Torchilin, V. P. (2006) · Annual Review of Biomedical Engineering · doi:10.1146/annurev.bioeng.8.061505.095735 · Cited by 548
Senes, A., Ubarretxena‐Belandia, I., & Engelman, D. M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.161280798 · Cited by 480
The structural biology of type I viral membrane fusion
Colman, P. M., & Lawrence, M. C. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1076 · Cited by 455
Nanotheranostics and image-guided drug delivery: current concepts and future directions
Lammers, T., Kiessling, F., Hennink, W. E., & Storm, G. (2010) · Molecular Pharmaceutics · doi:10.1021/mp100228v · Cited by 397
Mechanisms of pathogen entry through the endosomal compartments
Grüenberg, J., & van der Goot, F. G. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1959 · Cited by 375
Structural basis for membrane fusion by enveloped viruses
Weissenhorn, W., Dessen, A., Calder, L. J., Harrison, S. C., Skehel, J. J., & Wiley, D. C. (1999) · Molecular Membrane Biology · doi:10.1080/096876899294706 · Cited by 373
Asparagine-mediated self-association of a model transmembrane helix.
Lear, J. D., DeGrado, W. F., Choma, C. T., & Gratkowski, H. (2000) · Nature Structural Biology · doi:10.1038/72440 · Cited by 353
Self-citationEfficient and targeted delivery of siRNA in vivo
Shim, M. S., & Kwon, Y. J. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07904.x · Cited by 319
Computational Design of Peptides That Target Transmembrane Helices
Yin, H. H., Slusky, J. S. G., Berger, B. W., Walters, R. F. S., Vilaire, G., Игоревич, Л. Р., Lear, J. D., Caputo, G. A., BENNETT, J. S., & DeGrado, W. F. (2007) · Science · doi:10.1126/science.1136782 · Cited by 289
Self-citationHelix-packing motifs in membrane proteins
Walters, R. F. S., & DeGrado, W. F. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605878103 · Cited by 285
Self-citationTransport of protein toxins into cells: pathways used by ricin, cholera toxin and Shiga toxin
Sandvig, K., & van Deurs, B. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03182-4 · Cited by 272
Lear, J. D., & DeGrado, W. F. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48270-1 · Cited by 258
Self-citationSpatiotemporal controlled delivery of nanoparticles to injured vasculature
Chan, J. M., Zhang, L., Tong, R., Ghosh, D., Gao, W., Liao, G., Yuet, K. P., Gray, D. S., Rhee, J., Cheng, J., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914585107 · Cited by 253
Probing Designability via a Generalized Model of Helical Bundle Geometry
Grigoryan, G., & DeGrado, W. F. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.08.058 · Cited by 232
Self-citationHenry, S. M., ElSayed, M. E. H., Pirie, C. M., Hoffman, A. S., & Stayton, P. S. (2006) · Biomacromolecules · doi:10.1021/bm060143z · Cited by 217
Comparison of Helix Interactions in Membrane and Soluble α-Bundle Proteins
Eilers, M., Patel, A. B., Liu, W., & Smith, S. O. (2002) · Biophysical Journal · doi:10.1016/s0006-3495(02)75613-0 · Cited by 211
Abrams, M. T., Koser, M. L., Seitzer, J., Williams, S. C., DiPietro, M. A., Wang, W., Shaw, A. W., Mao, X., Jadhav, V., Davide, J. P., et al. (2010) · Molecular Therapy · doi:10.1038/mt.2009.208 · Cited by 209
Self-citationCronican, J. J., Thompson, D. B., Beier, K. T., McNaughton, B. R., Cepko, C. L., & Liu, D. R. (2010) · ACS Chemical Biology · doi:10.1021/cb1001153 · Cited by 205
Computational Design of Virus-Like Protein Assemblies on Carbon Nanotube Surfaces
Grigoryan, G., Kim, Y. H., Acharya, R., Axelrod, K., Jain, R. M., Willis, L. J., Drndić, M., Kikkawa, J. M., & DeGrado, W. F. (2011) · Science · doi:10.1126/science.1198841 · Cited by 204
Self-citationProtein Translocation through the Anthrax Toxin Transmembrane Pore is Driven by a Proton Gradient
Krantz, B. A., Finkelstein, A., & Collier, R. J. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.11.030 · Cited by 183
Kochendoerfer, G. G., Salom, D., Lear, J. D., Wilk-Orescan, R., Kent, S. B. H., & DeGrado, W. F. (1999) · Biochemistry · doi:10.1021/bi990720m · Cited by 178
Self-citationAnthrax toxin: the long and winding road that leads to the kill
Abrami, L., Reig, N., & van der Goot, F. G. (2004) · Trends in Microbiology · doi:10.1016/j.tim.2004.12.004 · Cited by 170
Recent trends in non‐viral vector‐mediated gene delivery
Pathak, A., Patnaik, S., & Gupta, K. C. (2009) · Biotechnology Journal · doi:10.1002/biot.200900161 · Cited by 170
An, M., Wijesinghe, D., Andreev, O. A., Reshetnyak, Y. K., & Engelman, D. M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1014403107 · Cited by 164
Interhelical hydrogen bonds and spatial motifs in membrane proteins: Polar clamps and serine zippers
Adamian, L., & Liang, J. (2002) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.10071 · Cited by 154
Repacking protein cores with backbone freedom: structure prediction for coiled coils.
Harbury, P. B., Tidor, B., & Kim, P. S. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.18.8408 · Cited by 149
From coiled coils to small globular proteins: Design of a native‐like three‐helix bundle
Bryson, J. W., Desjarlais, J. R., Handel, T. M., & DeGrado, W. F. (1998) · Protein Science · doi:10.1002/pro.5560070617 · Cited by 134
Self-citationBoeckle, S., Fahrmeir, J., Röedl, W., Ogris, M., & Wagner, E. (2006) · Journal of Controlled Release · doi:10.1016/j.jconrel.2006.02.002 · Cited by 132
Rafalski, M., Ortiz, A., Rockwell, A. L., van Ginkel, L. C., Lear, J. D., DeGrado, W. F., & Wilschut, J. (1991) · Biochemistry · doi:10.1021/bi00106a020 · Cited by 132
Self-citationThe design of antiparallel coiled coils
Oakley, M. G. (2001) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00232-3 · Cited by 131
Functional Protein Delivery into Neurons Using Polymeric Nanoparticles
Hasadsri, L., Kreuter, J., Hattori, H., Iwasaki, T., & George, J. M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m805956200 · Cited by 129
Computational design of water-soluble analogues of the potassium channel KcsA
Slovic, A. M., Kono, H., Lear, J. D., Saven, J. G., & DeGrado, W. F. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0306417101 · Cited by 114
Self-citationRuan, L., Zhang, H., Luo, H., Liu, J., Tang, F., Shi, Y., & Zhao, X. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900026106 · Cited by 114
Tucker, M. J., Getahun, Z., Nanda, V., DeGrado, W. F., & Gai, F. (2004) · Journal of the American Chemical Society · doi:10.1021/ja032015d · Cited by 111
Self-citationA de Novo Designed Protein Mimics the Native State of Natural Proteins
Raleigh, D. P., Betz, S. F., & DeGrado, W. F. (1995) · Journal of the American Chemical Society · doi:10.1021/ja00133a035 · Cited by 105
Self-citationDrug delivery systems for differential release in combination therapy
Zhang, H., Wang, G., & Yang, H. (2011) · Expert Opinion on Drug Delivery · doi:10.1517/17425247.2011.547470 · Cited by 103
Kwon, E. J., Bergen, J. M., & Pun, S. H. (2008) · Bioconjugate Chemistry · doi:10.1021/bc700448h · Cited by 101
Delivery systems for small molecule drugs, proteins, and DNA: the neuroscience/biomaterial interface
Whittlesey, K. J., & Shea, L. D. (2004) · Experimental Neurology · doi:10.1016/j.expneurol.2004.06.020 · Cited by 98
Tropomyosin: a model protein for studying coiled-coil and .alpha.-helix stabilization
Talbot, J. A., & Hodges, R. S. (1982) · Accounts of Chemical Research · doi:10.1021/ar00079a006 · Cited by 91
Recent Developments in Peptide-Based Nucleic Acid Delivery
Veldhoen, S., Laufer, S. D., & Restle, T. (2008) · International Journal of Molecular Sciences · doi:10.3390/ijms9071276 · Cited by 88
In vivo siRNA delivery with dendritic poly( l -lysine) for the treatment of hypercholesterolemia
Watanabe, K., Harada‐Shiba, M., Suzuki, A., Gokuden, R., Kurihara, R., Sugao, Y., Mori, T., Katayama, Y., & Niidome, T. (2009) · Molecular BioSystems · doi:10.1039/b900880b · Cited by 86
β-Cyclodextrin-Centered Star-Shaped Amphiphilic Polymers for Doxorubicin Delivery
Li, Q., Wang, R. J., Zheng, C., Jin, Y., & Jin, L. (2010) · Nanomedicine · doi:10.2217/nnm.09.108 · Cited by 86
Betz, S. F., Liebman, P. A., & DeGrado, W. F. (1997) · Biochemistry · doi:10.1021/bi961704h · Cited by 77
Self-citationDonald, J. E., Zhang, Y., Fiorin, G., Carnevale, V., Slochower, D. R., Gai, F., Klein, M. L., & DeGrado, W. F. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1019668108 · Cited by 69
Self-citationBartz, R., Fan, H., Zhang, J., Innocent, N., Cherrin, C., Beck, S. C., Pei, Y., Momose, A., Jadhav, V., Tellers, D. M., et al. (2011) · Biochemical Journal · doi:10.1042/bj20101021 · Cited by 63
Self-citationUnraveling the structures and modes of action of bacterial toxins
Lacy, D. B., & Stevens, R. C. (1998) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(98)80098-5 · Cited by 61
Medicinal Chemistry of siRNA Delivery
Stanton, M. G., & Colletti, S. L. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm1003914 · Cited by 60
Generalized Crick Equations for Modeling Noncanonical Coiled Coils
Offer, G., Hicks, M. R., & Woolfson, D. N. (2002) · Journal of Structural Biology · doi:10.1006/jsbi.2002.4448 · Cited by 59
Olson, D. L., Williksen, E. P., & Scheeline, A. (1995) · Journal of the American Chemical Society · doi:10.1021/ja00106a001 · Cited by 57
Role of Helix Nucleation in the Kinetics of Binding of Mastoparan X to Phospholipid Bilayers
Tang, J., Signarvic, R. S., DeGrado, W. F., & Gai, F. (2007) · Biochemistry · doi:10.1021/bi7018404 · Cited by 53
Self-citationCristian, L., Lear, J. D., & DeGrado, W. F. (2003) · Protein Science · doi:10.1110/ps.0378603 · Cited by 48
Self-citationMenikh, A., Saleh, M. T., Gariépy, J., & Boggs, J. M. (1997) · Biochemistry · doi:10.1021/bi970944+ · Cited by 45
Zhang, Y., Kulp, D. W., Lear, J. D., & DeGrado, W. F. (2009) · Journal of the American Chemical Society · doi:10.1021/ja904625b · Cited by 34
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Howorka, S. (2017) · Nature Nanotechnology · doi:10.1038/nnano.2017.99 · Cited by 295
Protein–protein interaction prediction with deep learning: A comprehensive review
Soleymani, F., Paquet, E., Viktor, H. L., Michalowski, W., & Spinello, D. (2022) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2022.08.070 · Cited by 204
The Role of Hypoxia-Induced miR-210 in Cancer Progression
Dang, K., & Myers, K. A. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms16036353 · Cited by 181
Computational Protein Design with Deep Learning Neural Networks
Wang, J., Cao, H., Zhang, J. Z. H., & Qi, Y. (2018) · Scientific Reports · doi:10.1038/s41598-018-24760-x · Cited by 164
De novo design of tunable, pH-driven conformational changes
Boyken, S. E., Benhaim, M. A., Büsch, F., Jia, M., Bick, M. J., Choi, H., Klima, J. C., Chen, Z., Walkey, C., Mileant, A., et al. (2019) · Science · doi:10.1126/science.aav7897 · Cited by 161
De novo protein design: how do we expand into the universe of possible protein structures?
Woolfson, D. N., Bartlett, G. J., Burton, A. J., Heal, J. W., Niitsu, A., Thomson, A. R., & Wood, C. W. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2015.05.009 · Cited by 160
Fusco, G., Simone, A. D., Arosio, P., Vendruscolo, M., Veglia, G., & Dobson, C. M. (2016) · Scientific Reports · doi:10.1038/srep27125 · Cited by 106
Towards functional de novo designed proteins
Dawson, W., Rhys, G. G., & Woolfson, D. N. (2019) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2019.06.011 · Cited by 71
Wang, Z., Zhang, J., Wang, Y., Zhou, J., Jiao, X., Han, M., Zhang, X., Hu, H., Su, R., Zhang, Y., et al. (2024) · ACS Nano · doi:10.1021/acsnano.4c02400 · Cited by 62
Self-citationComputational design of protein self-assembly
Norn, C., & André, I. (2016) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2016.04.002 · Cited by 59
A Novel Soluble Peptide with pH-Responsive Membrane Insertion
Nguyen, V. P., Alves, D. S., Scott, H. L., Davis, F. L., & Barrera, F. N. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00856 · Cited by 56
A De Novo Designed Coiled-Coil Peptide with a Reversible pH-Induced Oligomerization Switch
Lizatović, R., Aurelius, O., Stenström, O., Drakenberg, T., Akke, M., Logan, D. T., & André, I. (2016) · Structure · doi:10.1016/j.str.2016.03.027 · Cited by 48
Designed for life: biocompatible de novo designed proteins and components
Grayson, K. J., & Anderson, J. L. R. (2018) · Journal of The Royal Society Interface · doi:10.1098/rsif.2018.0472 · Cited by 36
From a pro-apoptotic peptide to a lytic peptide: One single residue mutation
Zhou, X., Zhang, Q., Tian, X.-B., Cao, Y., Liu, Z., Fan, R., Ding, X., Zhu, Z.-T., Chen, L., & Luo, S. (2016) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2016.05.012 · Cited by 35
Marginal protein stability drives subcellular proteome isoelectric point
Loell, K., & Nanda, V. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1809098115 · Cited by 25
Designing Covalently Linked Heterodimeric Four-Helix Bundles
Chino, M., Leone, L., Maglio, O., & Lombardi, A. (2016) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2016.05.036 · Cited by 24
Gao, X., Xu, K., Ahmad, N., Qin, L., & Li, C. (2021) · Biotechnology Journal · doi:10.1002/biot.202100151 · Cited by 23
De novo design of transmembrane nanopores
Qiao, D., Chen, Y., Tan, H., Zhou, R., & Feng, J. (2022) · Science China Chemistry · doi:10.1007/s11426-022-1354-5 · Cited by 11
De novo design of monomeric helical bundles for pH ‐controlled membrane lysis
Goldbach, N. M., Benna, I., Wicky, B. I. M., Croft, J. T., Carter, L. P., Bera, A. K., Nguyen, H., Kang, A., Sankaran, B., Yang, E. C., et al. (2023) · Protein Science · doi:10.1002/pro.4769 · Cited by 10
Notari, E., Wood, C. W., & Michel, J. (2025) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.4c01695 · Cited by 4
Generating the Fancy Protein Basket with De Novo and Combinatorial Approaches
Poluri, K. M., & Gulati, K. (2016) · SpringerBriefs in applied sciences and technology · doi:10.1007/978-981-10-2732-1_4 · Cited by 3
De novo design and synthesis of biomolecules
Paul, S. S., Dhali, D., Yaseen, Y., Basu, U., Pal, S., Mohammed, N. Y., & Trabelsi, H. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-824469-2.00020-8
Metadata
- Authors
- Zhang, Y., Bartz, R., Grigoryan, G., Bryant, M., Aaronson, J., Beck, S., Innocent, N., Klein, L., Procopio, W., Tucker, T., Jadhav, V., Tellers, D. M., & DeGrado, W. F.
- Affiliations
- University of Pennsylvania (US)
- Merck & Co., Inc., Rahway, NJ, USA (United States) (US)
- University of California, San Francisco (US)
- Corresponding author
- Tellers, David M.
- DeGrado, William F.
- ORCID
- Venue
- ACS Chemical Biology
- Publisher
- American Chemical Society (ACS)
- Published
- 2015-01-28
- Volume
- 10
- Issue
- 4
- Pages
- 1082-1093
- ISSN
- 1554-8929 (ISSN-L)
- 1554-8937
- PMC
- PMC4843813
- OpenAlex
- W2086480986
- Cited by
- 23
- References
- 64
- Citations by year
- 2025: 1 · 2024: 2 · 2023: 1 · 2022: 3 · 2021: 1 · 2019: 2 · 2018: 3 · 2017: 1 · 2016: 6 · 2015: 3
- FWCI
- 1.88
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- ACS Chemical Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM054616)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Interference and Gene Delivery
- Physical Sciences › Materials Science › Biomaterials › Nanoparticle-Based Drug Delivery
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Keywords
- membrane insertion, intracellular drug delivery, ATP release, erythrocytes, cytosolic delivery
- MeSH terms
- Adenosine Triphosphate, Amino Acid Sequence, Cell Membrane, Chromatography, Gel, Circular Dichroism, Erythrocytes, Hemolysis, Humans, Hydrogen-Ion Concentration, Lipid Bilayers, Molecular Sequence Data, Peptides, Solubility, Spectrometry, Fluorescence, Tryptophan, Drug Design, Protein Engineering, MicroRNAs
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review